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Database: UniProt
Entry: B3SCQ7_TRIAD
LinkDB: B3SCQ7_TRIAD
Original site: B3SCQ7_TRIAD 
ID   B3SCQ7_TRIAD            Unreviewed;       700 AA.
AC   B3SCQ7;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=SH2 domain-containing protein {ECO:0000259|PROSITE:PS50001};
GN   ORFNames=TRIADDRAFT_62062 {ECO:0000313|EMBL:EDV19496.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV19496.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV19496.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV19496.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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DR   EMBL; DS985272; EDV19496.1; -; Genomic_DNA.
DR   RefSeq; XP_002118013.1; XM_002117977.1.
DR   AlphaFoldDB; B3SCQ7; -.
DR   STRING; 10228.B3SCQ7; -.
DR   EnsemblMetazoa; TriadT62062; TriadP62062; TriadG62062.
DR   GeneID; 6759226; -.
DR   KEGG; tad:TRIADDRAFT_62062; -.
DR   CTD; 6759226; -.
DR   HOGENOM; CLU_393978_0_0_1; -.
DR   InParanoid; B3SCQ7; -.
DR   OrthoDB; 3681543at2759; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   CDD; cd00173; SH2; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   PANTHER; PTHR19969:SF5; ADAPTER MOLECULE CRK; 1.
DR   PANTHER; PTHR19969; SH2-SH3 ADAPTOR PROTEIN-RELATED; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT   DOMAIN          540..632
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          497..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  80438 MW;  6DD5E2EE8E1BA2C0 CRC64;
     MDSDDDIYDC MLESSVKLVY DRILPKLERQ LPTKNFCKGA FKLGIIDYDK VLTASHEHIS
     PDINRKILEY IDSEQLDDIK DWLSIMFDDE KCRPIAYEFI NELSEWKLEE LVENINIKDG
     YILISDKLIS VSKLDSVQMD VDEPVIIVQD SISRKSFPIN KDHSVDVPIH AEDIKHKVNV
     SVPFPIHYRP MSTEIDIFPL VTRFTAMASA SLVIKTWLQL PDSTSDQGNI RDCQLTCWIP
     HYKQIKQLFC KSEKSVQQND KIIVARRINS DSTKFTEIGT KFSIDENKAT DDGVVVKCNC
     SYQSVINWFW KIPQWLLDAA RLGPKYYYDY FRYPVQYFVG VKPMKDKPGH FTLIALVKNI
     RCPLPSRIGD ELELLASSGD ETRLLSSGRL QINLAGDIKP LNGLIWVELL NKIAYFDGMY
     SVTQFACMGH FDADNGIYSK GSVEFRYIDP GPNCHPDASN PDYNVENESV VVEFSYAIDH
     EMTRKYSIIR GNVSDPETTG KVDARSPQPD PFTDTPMHNS KELSQNLSLI DSIEDTRHLW
     YQEDMTKVNA IVFLQDQPIG TFVVRKSTRH HCEAISVKVT VDGNIGHFLF KNNSNEWSIA
     DFERKFVSLE DLLTHYTNNK DKELQVKLRF PRPIHSNAKV EPETQSLPGE ISDCTMQHVS
     IQDYNEVSNL EKFEYILSDS EENTGLSIEL WYQFTLIISK
//
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